메뉴 건너뛰기




Volumn 26, Issue 1, 2003, Pages 27-32

A common architecture for K+ channels and ionotropic glutamate receptors?

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR; IONOTROPIC RECEPTOR; POTASSIUM CHANNEL; POTASSIUM ION;

EID: 0037213506     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(02)00010-3     Document Type: Article
Times cited : (102)

References (39)
  • 2
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science. 280:1998;69-77.
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 3
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., et al. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:2002;515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1
  • 4
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler R., et al. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature. 415:2002;287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1
  • 5
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G., et al. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:1998;2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1
  • 6
    • 0029012475 scopus 로고
    • Pore-loops: An emerging theme in ion channel structure
    • MacKinnon R. Pore-loops: an emerging theme in ion channel structure. Neuron. 14:1995;889-892.
    • (1995) Neuron , vol.14 , pp. 889-892
    • MacKinnon, R.1
  • 7
    • 0026347866 scopus 로고
    • Similarities in amino acid sequences of Drosophila eag and cyclic nucleotide-gated channels
    • Guy H.R., et al. Similarities in amino acid sequences of Drosophila eag and cyclic nucleotide-gated channels. Science. 254:1991;730.
    • (1991) Science , vol.254 , pp. 730
    • Guy, H.R.1
  • 9
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo Z.G., Oswald R.E. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18:1995;161-168.
    • (1995) Trends Neurosci. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 10
    • 0032780667 scopus 로고    scopus 로고
    • + channels and symporters
    • + channels and symporters. Biophys. J. 77:1999;775-788.
    • (1999) Biophys. J. , vol.77 , pp. 775-788
    • Durell, S.R.1
  • 11
    • 0032912771 scopus 로고    scopus 로고
    • The glutamate receptor ion channels
    • Dingledine R., et al. The glutamate receptor ion channels. Pharmacol. Rev. 51:1999;7-61.
    • (1999) Pharmacol. Rev. , vol.51 , pp. 7-61
    • Dingledine, R.1
  • 12
    • 0029071823 scopus 로고
    • Structural conservation of ion conduction pathways in K channels and glutamate receptors
    • Wood M.W., et al. Structural conservation of ion conduction pathways in K channels and glutamate receptors. Proc. Natl Acad. Sci. U.S.A. 92:1995;4882-4886.
    • (1995) Proc. Natl Acad. Sci. U.S.A. , vol.92 , pp. 4882-4886
    • Wood, M.W.1
  • 13
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin A., Akabas M.H. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1995;1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 14
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • Wo Z.G., Oswald R.E. Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation. Proc. Natl Acad. Sci. U.S.A. 91:1994;7154-7158.
    • (1994) Proc. Natl Acad. Sci. U.S.A. , vol.91 , pp. 7154-7158
    • Wo, Z.G.1    Oswald, R.E.2
  • 15
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann M., et al. N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron. 13:1994;1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1
  • 16
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining reentrant membrane loop
    • Bennett J.A., Dingledine R. Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop. Neuron. 14:1995;373-384.
    • (1995) Neuron , vol.14 , pp. 373-384
    • Bennett, J.A.1    Dingledine, R.2
  • 17
    • 0025266744 scopus 로고
    • Searching through sequence databases
    • Doolittle R.F. Searching through sequence databases. Methods Enzymol. 183:1990;99-110.
    • (1990) Methods Enzymol. , vol.183 , pp. 99-110
    • Doolittle, R.F.1
  • 18
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • Chen G.Q., et al. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature. 402:1999;817-821.
    • (1999) Nature , vol.402 , pp. 817-821
    • Chen, G.Q.1
  • 19
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • Ochman H., et al. Lateral gene transfer and the nature of bacterial innovation. Nature. 405:2000;299-304.
    • (2000) Nature , vol.405 , pp. 299-304
    • Ochman, H.1
  • 20
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine-accessibility method
    • Karlin A., Akabas M.H. Substituted-cysteine-accessibility method. Methods Enzymol. 293:1998;123-136.
    • (1998) Methods Enzymol. , vol.293 , pp. 123-136
    • Karlin, A.1    Akabas, M.H.2
  • 21
    • 0035876181 scopus 로고    scopus 로고
    • Channel-lining residues of the AMPA receptor M2 segment: Structural environment of the Q/R site and identification of the selectivity filter
    • Kuner T., et al. Channel-lining residues of the AMPA receptor M2 segment: structural environment of the Q/R site and identification of the selectivity filter. J. Neurosci. 21:2001;4162-4172.
    • (2001) J. Neurosci. , vol.21 , pp. 4162-4172
    • Kuner, T.1
  • 22
    • 0030220889 scopus 로고    scopus 로고
    • Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines
    • Kuner T., et al. Structure of the NMDA receptor channel M2 segment inferred from the accessibility of substituted cysteines. Neuron. 17:1996;343-352.
    • (1996) Neuron , vol.17 , pp. 343-352
    • Kuner, T.1
  • 23
    • 0035003258 scopus 로고    scopus 로고
    • + channels examined by scanning mutagenesis
    • + channels examined by scanning mutagenesis. J. Gen. Physiol. 117:2001;345-360.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 345-360
    • Panchenko, V.A.1
  • 24
    • 0028941130 scopus 로고
    • + channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis
    • + channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis. Biophys. J. 68:1995;900-905.
    • (1995) Biophys. J. , vol.68 , pp. 900-905
    • Kürz, L.L.1
  • 25
    • 0029070117 scopus 로고
    • + pore structure revealed by reporter cysteines at inner and outer surfaces
    • + pore structure revealed by reporter cysteines at inner and outer surfaces. Neuron. 14:1995;1055-1063.
    • (1995) Neuron , vol.14 , pp. 1055-1063
    • Pascual, J.M.1
  • 26
    • 0030795112 scopus 로고    scopus 로고
    • + channel
    • + channel. Neuron. 19:1997;175-184.
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, Y.1
  • 27
    • 0030051784 scopus 로고    scopus 로고
    • Agitoxin footprinting the shaker potassium channel pore
    • Gross A., MacKinnon R. Agitoxin footprinting the shaker potassium channel pore. Neuron. 16:1996;399-406.
    • (1996) Neuron , vol.16 , pp. 399-406
    • Gross, A.1    MacKinnon, R.2
  • 28
    • 0029887686 scopus 로고    scopus 로고
    • Differential contribution of the NR1- and NR2A-subunits to the selectivity filter of recombinant NMDA receptor channels
    • Wollmuth L.P., et al. Differential contribution of the NR1- and NR2A-subunits to the selectivity filter of recombinant NMDA receptor channels. J. Physiol. (Lond.). 491:1996;779-797.
    • (1996) J. Physiol. (Lond.) , vol.491 , pp. 779-797
    • Wollmuth, L.P.1
  • 29
    • 0004054951 scopus 로고    scopus 로고
    • P. Jonas, & H. et al. Monyer. Springer
    • Kuner T., et al. Jonas P., Monyer H., et al. Handbook of Experimental Pharmacology. Handbook of Experimental Pharmacology. Vol. 141:1999;Springer.
    • (1999) Handbook of Experimental Pharmacology , vol.141
    • Kuner, T.1
  • 30
    • 0028029407 scopus 로고
    • Ion permeation properties of the cloned mouse ε2/ζ1 NMDA receptor channel
    • Tsuzuki K., et al. Ion permeation properties of the cloned mouse ε2/ζ1 NMDA receptor channel. Brain Res. Mol. Brain Res. 26:1994;37-46.
    • (1994) Brain Res. Mol. Brain Res. , vol.26 , pp. 37-46
    • Tsuzuki, K.1
  • 31
    • 0026675738 scopus 로고
    • Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels
    • Dingledine R., et al. Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels. J. Neurosci. 12:1992;4080-4087.
    • (1992) J. Neurosci. , vol.12 , pp. 4080-4087
    • Dingledine, R.1
  • 33
    • 0033380377 scopus 로고    scopus 로고
    • The structure of aquaporin-1 at 4.5-A resolution reveals short α-helices in the center of the monomer
    • Mitsuoka K., et al. The structure of aquaporin-1 at 4.5-A resolution reveals short α-helices in the center of the monomer. J. Struct. Biol. 128:1999;34-43.
    • (1999) J. Struct. Biol. , vol.128 , pp. 34-43
    • Mitsuoka, K.1
  • 34
    • 0033761347 scopus 로고    scopus 로고
    • Structure of a glycerol-conducting channel and the basis for its selectivity
    • Fu D., et al. Structure of a glycerol-conducting channel and the basis for its selectivity. Science. 290:2000;481-486.
    • (2000) Science , vol.290 , pp. 481-486
    • Fu, D.1
  • 35
    • 3042695848 scopus 로고    scopus 로고
    • A family of putative Kir potassium channels in prokaryotes
    • Durell S.R., Guy H.R. A family of putative Kir potassium channels in prokaryotes. BMC Evol. Biol. 1:2001;14.
    • (2001) BMC Evol. Biol. , vol.1 , pp. 14
    • Durell, S.R.1    Guy, H.R.2
  • 36
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • Jiang Y., et al. The open pore conformation of potassium channels. Nature. 417:2002;523-526.
    • (2002) Nature , vol.417 , pp. 523-526
    • Jiang, Y.1
  • 37
    • 0033103522 scopus 로고    scopus 로고
    • NMDAR channel segments forming the extracellular vestibule inferred from the accessibility of substituted cysteines
    • Beck C., et al. NMDAR channel segments forming the extracellular vestibule inferred from the accessibility of substituted cysteines. Neuron. 22:1999;559-570.
    • (1999) Neuron , vol.22 , pp. 559-570
    • Beck, C.1
  • 38
    • 0037012062 scopus 로고    scopus 로고
    • Molecular rearrangements of the extracellular vestibule in NMDAR channels during gating
    • Sobolevsky A.I., et al. Molecular rearrangements of the extracellular vestibule in NMDAR channels during gating. Neuron. 33:2002;75-85.
    • (2002) Neuron , vol.33 , pp. 75-85
    • Sobolevsky, A.I.1
  • 39
    • 0030663654 scopus 로고    scopus 로고
    • Prokaryotes offer hope for potassium channel structural studies
    • MacKinnon R., Doyle D.A. Prokaryotes offer hope for potassium channel structural studies. Nat. Struct. Biol. 4:1997;877-879.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 877-879
    • MacKinnon, R.1    Doyle, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.